STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
from curated databases
Hypothetical protein (224 aa)
Predicted Functional Partners:
Hypothetical protein (147 aa)
Class V aminotransferase (404 aa)
Aminotransferase (436 aa)
Class V aminotransferase (376 aa)
Oxygen-independent coproporphyrinogen III oxidase (376 aa)
tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (430 aa)
ATP-NAD kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2’-hydroxyl of the adenosine moiety of NAD to yield NADP (288 aa)
UDP-N-acetylmuramoylalanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (450 aa)
Your Current Organism:
Porphyromonas gingivalis W83
NCBI taxonomy Id: 242619 Other names: P. gingivalis W83, Porphyromonas gingivalis W83, Porphyromonas gingivalis str. W83, Porphyromonas gingivalis strain W83
ATP-NAD kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2’-hydroxyl of the adenosine moiety of NAD to yield NADP